Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-12-10
pubmed:databankReference
pubmed:abstractText
The zinc finger regions of the Aspergillus nidulans PacC transcription factor, mediating regulation of gene expression by ambient pH, and the Saccharomyces cerevisiae Rim1p transcription factor, mediating control of meiosis and invasiveness, are homologous and both transcription factors undergo proteolytic processing of the C-terminus for conversion to the functional form. In both cases, functioning of a signal transduction pathway involving several gene products is a necessary prerequisite for processing. We now show that the Aspergillus PalI pH signal transduction component is homologous to the Saccharomyces Rim9p meiotic signal transduction component throughout a region containing four hydrophobic, putative membrane-spanning segments. This suggests that PalI might be a membrane sensor for ambient pH. Deletion of the palI gene established that the less extreme phenotype of palI mutations compared with mutations in the other five genes of the pH signalling pathway is a general feature of palI mutations.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonucleases, Type II..., http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PacC protein, Aspergillus, http://linkedlifedata.com/resource/pubmed/chemical/RIM101 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors, http://linkedlifedata.com/resource/pubmed/chemical/endodeoxyribonuclease HpaI, http://linkedlifedata.com/resource/pubmed/chemical/endodeoxyribonuclease SacI
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0950-382X
pubmed:author
pubmed:issnType
Print
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
259-64
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9791171-Amino Acid Sequence, pubmed-meshheading:9791171-Aspergillus nidulans, pubmed-meshheading:9791171-Base Sequence, pubmed-meshheading:9791171-Blotting, Northern, pubmed-meshheading:9791171-Cloning, Molecular, pubmed-meshheading:9791171-DNA-Binding Proteins, pubmed-meshheading:9791171-Deoxyribonucleases, Type II Site-Specific, pubmed-meshheading:9791171-Fungal Proteins, pubmed-meshheading:9791171-Hydrogen-Ion Concentration, pubmed-meshheading:9791171-Meiosis, pubmed-meshheading:9791171-Membrane Proteins, pubmed-meshheading:9791171-Molecular Sequence Data, pubmed-meshheading:9791171-Mutation, pubmed-meshheading:9791171-Repressor Proteins, pubmed-meshheading:9791171-Saccharomyces cerevisiae, pubmed-meshheading:9791171-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9791171-Sequence Homology, Amino Acid, pubmed-meshheading:9791171-Signal Transduction, pubmed-meshheading:9791171-Transcription Factors
pubmed:year
1998
pubmed:articleTitle
Putative membrane components of signal transduction pathways for ambient pH regulation in Aspergillus and meiosis in saccharomyces are homologous.
pubmed:affiliation
Department of Infectious Diseases, Imperial College School of Medicine at Hammersmith Hospital, Ducane Road, London W12 ONN, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't